| Literature DB >> 19351885 |
Takeshi Takahashi1, Natsuko Inoue-Kashino, Shin-Ichiro Ozawa, Yuichiro Takahashi, Yasuhiro Kashino, Kazuhiko Satoh.
Abstract
Photosystem II (PS II) complexes are membrane protein complexes that are composed of >20 distinct subunit proteins. Similar to many other membrane protein complexes, two PS II complexes are believed to form a homo-dimer whose molecular mass is approximately 650 kDa. Contrary to this well known concept, we propose that the functional form of PS II in vivo is a monomer, based on the following observations. Deprivation of lipids caused the conversion of PS II from a monomeric form to a dimeric form. Only a monomeric PS II was detected in solubilized cyanobacterial and red algal thylakoids using blue-native polyacrylamide gel electrophoresis. Furthermore, energy transfer between PS II units, which was observed in the purified dimeric PS II, was not detected in vivo. Our proposal will lead to a re-evaluation of many crystallographic models of membrane protein complexes in terms of their oligomerization status.Entities:
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Year: 2009 PMID: 19351885 PMCID: PMC2708856 DOI: 10.1074/jbc.M109.000372
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157